Purification and Immunological Analysis of Phospholipase D from Castor Bean Endosperm

Wang, Xuemin; Dyer, James H.; Zheng, Li

doi:10.1006/abbi.1993.1541

Cited by 92 publications

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“…The cloning of cDNA for higher eukaryote PLD was initially reported by Wang et al (18), who isolated the cDNA for castor bean (Ricinus communis) PLD by using oligonucleotide probes based on the amino-terminal amino acid sequence of the purified protein (19). Using sequence similarity to castor bean PLD, the Saccharomyces cerevisiae SPO14 gene (20) was identified as the yeast PLD gene (21,22).…”

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Cloning, Expression, and Characterization of a Novel Phospholipase D Complementary DNA from Rat Brain

Kodaki

Yamashita

1997

Journal of Biological Chemistry

219

165

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Here we report the cloning and characterization of cDNA for a different type of PLD (rat PLD2 (rPLD2)) from rat brain. We synthesized highly degenerate amplimers corresponding to the conserved regions of eukaryote PLDs and performed polymerase chain reaction on a rat brain cDNA library. Using the amplified sequence as the probe, we cloned a rat brain cDNA clone that contained an open reading frame of 933 amino acids with an M r of 105,992. The deduced amino acid sequence showed significant similarity to hPLD1 with a large deletion in the middle of the sequence. When the sequence was expressed in the fission yeast Schizosaccharomyces pombe, PLD activity was greatly increased. The activity was markedly stimulated by phosphatidylinositol 4,5-bisphosphate, but not by ADPribosylation factor 1 and RhoA. Rat brain cytosol known to stimulate small GTP-binding protein-dependent PLD did not stimulate rPLD2 expressed in S. pombe. The transcript was detected at significant levels in brain, lung, heart, kidney, stomach, small intestine, colon, and testis, but at low levels in thymus, liver, and muscle. Only a negligible level was found in spleen and pancreas. Thus rPLD2 is a novel type of PLD dependent on phosphatidylinositol 4,5-bisphosphate, but not on the small GTP-binding proteins ADP-ribosylation factor 1 and RhoA. Phospholipase D (PLD)1 catalyzes the hydrolysis of phosphatidylcholine (PC) to phosphatidic acid and choline (1). A variety of signal molecules such as hormones, neurotransmitters, and growth factors are known to induce the activation of PLD in a wide range of cell types. Hence PLD is implicated in a broad spectrum of physiological processes and diseases, including metabolic regulation, inflammation, secretion, mitogenesis, oncogenesis, neural and cardiac stimulation, diabetes, and senescence (for reviews, see Ref.2). Despite its crucial importance in signal transduction, the molecular structure and characteristics of PLD enzyme are only poorly understood.Multiple PLD isoforms exist in mammalian tissues. Several factors were reported to stimulate PLD activity in vitro, including unsaturated fatty acid (3), phosphatidylinositol 4,5-bisphosphate (PIP 2 ) (4), monomeric GTP-binding proteins (G proteins) such as ADP-ribosylation factor 1 (ARF1) (5, 6) and RhoA (7, 8), protein kinase C (9), and calmodulin (10). Massenburg et al. (11) showed that two major forms of PLD activity in rat brain membranes can be separated into ARF-dependent and oleate-dependent enzymes, clearly indicating that these are distinct isoforms. Both oleate-dependent and ARF-dependent types of PLD were recently highly purified from pig lung and brain, respectively (12, 13). In addition, there may be multiple forms of small G protein-dependent PLD including ARF-sensitive, RhoA-sensitive, and ARF-, RhoA-sensitive PLDs. Siddiqi et al. (14) reported that the cytosolic fraction of HL-60 cells contained a soluble PLD activated by ARF, but not RhoA. Malcolm et al. (8) showed rat liver plasma membrane PLD to be sensitive to RhoA, but not to ARF. PL...

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confidence: 99%

Cloning, Expression, and Characterization of a Novel Phospholipase D Complementary DNA from Rat Brain

Kodaki

Yamashita

1997

Journal of Biological Chemistry

219

165

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“…PLD has been found in soluble and membrane-associated fractions in various plants, and its relative distribution between these two fractions varies, depending on the species, tissues, and developmental stages of the tissues (Heller, 1978;Wang et al, 1993;Dyer et al, 1994). An early experiment using differential centrifugation suggested that PLD was associated with plastids in severa1 plant species (Kates, 1955).…”

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Intracellular Localization of Phospholipase D in Leaves and Seedling Tissues of Castor Bean

Paulsen

Ryu

et al. 1996

Plant Physiology

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The intracellular distribution of phospholipase D (PLD; EC 3.1.4.4) i n castor bean (Ricinus communis L.) tissues was investigated by subcellular fractionation and by immuno-electron microscopy. Centrifugal fractionation revealed that most PLD i n young leaves was soluble, whereas in mature leaves a majority of PLD was associated with microsomal membranes. Further separation of microsomal membranes by a two-phase partitioning system indicated that PLD was associated with both plasma and intracellular membranes. Sucrose gradient separation of intracellular membranes showed PLD present i n the endoplasmic reticulum, a submicrosomal band, and in soluble fractions but not in mitochondria and glyoxysomes of postgermination endosperm. lmmunocytochemical studies found high gold labeling in vacuoles in young leaves, suggesting that the high leve1 of soluble PLD i n young leaves is due to release of PLD from vacuoles during tissue disruption. I n addition to the labeling in vacuoles, gold particles were also found in the cytoplasmic matrices and plasma membrane i n leaves and i n 2-d postgermination seedlings. Collectively, these results show that PLD in castor bean leaf and seedling tissues is localized in the vacuole and is associated with the endoplasmic reticulum and plasma membrane and that the relative distribution between the soluble and membrane compartments changes during castor bean leaf development.

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“…PLD is active in many plant tissues, but its physiological significance in plant growth and development is unclear (Heller, 1978;Wang, 1993). Changes in PLD activity were observed in a number of physiological processes, including various stress injuries (Yoshida, 1979;Chetal et al, 1982;Willemot, 1983), senescence , and seed aging and germination (Herman and Chrispeels, 1980;Di Nola and Mayer, 1986;Lee, 1989;Samama and Pearce, 1993;Wang et al, 1993). It has been proposed that PLD-mediated hydrolysis is a first step in membrane deterioration in senescing carnation flowers, tomato fruits, cabbage leaves, y-irradiated cauliflower florets, and aging cucumber and onion seeds Thompson et al, 1987;Cheour et al, 1992;McCormac et al, 1993;Samama and Pearce, 1993;Voisine et al, 1993).…”

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Expression of Phospholipase D during Castor Bean Leaf Senescence

Ryu

Wang

1995

Plant Physiol.

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Membrane deterioration in plant senescence is commonly associated with progressive decreases in membrane phospholipid content. This study investigated the expression and regulation of phospholipase D (PLD; EC 3.1.4.4) during senescence in castor bean (Ricinus communis L. cv Hale) leaf discs. The rate of leaf senescence was accelerated by 5 0 p~ abscisic acid and was attenuated by 50 p~ cytokinin during incubation at 23°C for up to 5 d. Leaf senescence was indicated by decreases in the content of total proteins, chlorophyll, and phospholipids. PLD activity in both membraneassociated and cytosolic fractions showed a gradual increase in the absence of phytohormones. Abscisic acid stimulated an increase in membrane-associated PLD and had little effect on the soluble form. On the other hand, cytokinin retarded the increase in membraneassociated PLD. lmmunoblotting analysis using PLD-specific antibodies revealed that the changes in PLD activity were correlated with those of PLD protein. Analysis of PLD by nondenaturing PACE showed the appearance of a PLD structural variant, PLD 3, i n abscisic acid-treated leaf discs. Northern blotting analysis using a PLD cDNA probe revealed an increase in PLD mRNA in senescing leaf discs. These data indicate complex mechanisms for the regulation of PLD during senescence, which include increases in membrane-associated PLD, differential expression of PLD isoforms, and changes in amounts of PLD protein and mRNA. Such controlled expression points to a role for PLD i n membrane deterioration and plant senescence.PLD (EC 3.1.4.4) hydrolyzes glycerophospholipids at the terminal phosphodiesteric bond, leading to the formation of PA and a free amino alcohol group. PLD is active in many plant tissues, but its physiological significance in plant growth and development is unclear (Heller, 1978;Wang, 1993). Changes in PLD activity were observed in a number of physiological processes, including various stress injuries (Yoshida, 1979;Chetal et al., 1982;Willemot, 1983), senescence , and seed aging and germination (Herman and Chrispeels, 1980;Di Nola and Mayer, 1986;Lee, 1989;Samama and Pearce, 1993;Wang et al., 1993). It has been proposed that PLD-mediated hydrolysis is a first step in membrane deterioration in senescing carnation flowers, tomato fruits, cabbage leaves, y-irradiated cauliflower florets, and aging cucumber and onion seeds Thompson et al., 1987;Cheour et al., 1992;McCormac et al., 1993;Samama and Pearce, 1993;Voisine et al., 1993). The resulting PLD product, PA, is further hydrolyzed by PA phosphatase and acyl hydrolases, followed by lipoxygenase. These reactions lead to the formation of oxy-free radicals and lipid peroxides that may cause membrane deterioration. Increased PLD activity may also result directly in membrane destabilization, since PA favors nonlamellar phase formation (Israelachvilli et al., 1980;Samama and Pearce, 1993).Crucial to the understanding of the cellular role for PLD is its regulatory mechanism and expression during plant growth and development. Decreases in...

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Purification and Immunological Analysis of Phospholipase D from Castor Bean Endosperm

Cited by 92 publications

References 0 publications

Cloning, Expression, and Characterization of a Novel Phospholipase D Complementary DNA from Rat Brain

Cloning, Expression, and Characterization of a Novel Phospholipase D Complementary DNA from Rat Brain

Intracellular Localization of Phospholipase D in Leaves and Seedling Tissues of Castor Bean

Expression of Phospholipase D during Castor Bean Leaf Senescence

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